SPT15/YER148W Summary Help

Standard Name SPT15
Systematic Name YER148W
Alias BTF1 , TBP1
Feature Type ORF, Verified
Description TATA-binding protein; general transcription factor that interacts with other factors to form the preinitiation complex at promoters, essential for viability (1, 2 and see Summary Paragraph)
Name Description SuPpressor of Ty
Gene Product Alias TBP
Chromosomal Location
ChrV:465303 to 466025 | ORF Map | GBrowse
Genetic position: 110 cM
Gene Ontology Annotations All SPT15 GO evidence and references
  View Computational GO annotations for SPT15
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 72 genes
Classical genetics
Large-scale survey
568 total interaction(s) for 165 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 163
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 164
  • Biochemical Activity: 2
  • Co-crystal Structure: 9
  • Co-fractionation: 5
  • Co-localization: 25
  • Co-purification: 6
  • Far Western: 1
  • PCA: 3
  • Protein-peptide: 1
  • Reconstituted Complex: 90
  • Two-hybrid: 11

Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Rescue: 40
  • Negative Genetic: 2
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 2
  • Synthetic Growth Defect: 9
  • Synthetic Lethality: 14
  • Synthetic Rescue: 18

Expression Summary
Length (a.a.) 240
Molecular Weight (Da) 27,003
Isoelectric Point (pI) 10.16
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrV:465303 to 466025 | ORF Map | GBrowse
Genetic position: 110 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..723 465303..466025 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000950

SPT15 encodes TATA-binding protein (TBP), an essential general transcription factor involved in directing the transcription of genes by the three nuclear RNA polymerases, I, II, and III (3, 4). TBP is a component of the polymerase I core factor, TFIID, and TFIIIB, which are complexes required for delivering polymerases I, II, and III, respectively, to transcription start sites (reviewed in 5, 6, 7). TBP localizes to promoter sites either by direct binding to a TATA box motif (TATA(a/t)A(a/t)N; 8, 9) or through recruitment by other complexes such as UAF, SAGA, or TFIIIC (reviewed in 5, 6, 7).

TBP is one of the few transcription factors highly conserved among all eukaryotes and archaea, though it is not found in eubacteria. Across eukaryotes, the 180-residue core domain shares 80% sequence identity (10). In humans, trinucleotide expansions in TBP lead to the Huntington-like neurological disorder Spinocerebellar Ataxia-17 (OMIM) (11).

In S. cerevisiae, the TBP polypeptide is a 240-residue molecule with a 60 amino acid N-terminal region that is divergent among eukaryotes, and a highly-conserved C-terminal core domain (12). The N-terminal domain has been suggested to inhibit TBP/DNA interaction and to mediate TBP/protein interaction (13). The C-terminus is pseudo-symmetric and saddle-shaped, with amino and carboxyl-terminal stirrups flanking a concave/convex surface. The concave side of TBP primarily binds to the minor groove of DNA, which unwinds the double-helix and induces a dramatic bend in the DNA (14, 9 and references contained therein). The convex side is the site of interaction for many transcriptional activators and repressors (15). The C-terminal stirrup and the concave side of TBP are involved in the formation of TBP homodimers, which serves as a self-regulatory mechanism as these dimers are inactive and must disassociate before the protein is able to bind DNA (16).

Levels of transcription are often regulated by targeting TBP. For example, dimer disassociation and TBP/promoter association are considered the rate-limiting steps in the formation of transcriptional pre-initiation complexes; the slow rate of this process serves to prevent unregulated gene expression (17, 18). Many transcriptional activators, such as the SAGA and mediator complexes, stimulate transcription by facilitating TBP binding to the TATA box (19, reviewed in 20) while transcriptional repressors such as histones, Mot1p, and negative cofactor 2 impede this interaction (21, 22).

As a component of the polymerase I core factor, TFIID, and TFIIIB, TBP is essential for positioning the appropriate RNA polymerase at the transcription start site. Polymerase I (Pol I), which directs the transcription of rRNA, localizes to the promoters of ribosomal genes bound by the upstream activating factor (UAF) and the core factor (CF) (reviewed in 5, 23). UAF binds to a pol I promoter in a sequence-specific manner and then recruits CF to a site in the promoter known as the core domain (23). The core domain overlaps the site of transcription initiation so CF is able to position pol I over the transcription start site and facilitate multiple rounds of transcription (24). Along with TBP, CF is comprised of the subunits Rrn6p, Rrn7p, and Rrn11p (25 and references contained therein). Although initial TBP association with CF is functional but not stable, this interaction is stabilized upon contact with UAF, which is mediated by protein-protein interaction between TBP and the UAF subunit Rrn9p (23).

TFIID is a transcription factor complex that is required for RNAPII-mediated transcription of protein-coding genes and some small nuclear RNAs (reviewed in 26). The complex is composed of Spt15p (TATA binding protein; TBP) and 14 TBP-associated factors (TAFs): Taf1p, Taf2p, Taf3p, Taf4p, Taf5p, Taf6p, Taf7p, Taf8p, Taf9p, Taf10p, Taf11p, Taf12p, Taf13p, Taf14p (27, 28). The TFIID complex is required for basal transcription, but some individual subunits regulate the activated transcription of a subset of genes (29, 30, 31, 32, 33). Recognition of promoter DNA by the TFIID complex is required for the formation of the preinitation complex (PIC) during transcription initiation (34, 35). The interaction between the TFIID complex and the promoter is stabilized by TFIIA (35, 36). The recruitment of TFIID to promoters is dependent on an upstream activating sequence in the promoter region (37).

The TFIIIB complex is a initiation factor for RNA polymerase III, which transcribes tRNAs, most small nuclear RNAs, and 5S rRNA (reviewed in 7). TFIIIB, comprised of TBP (Spt15p), Brf1p, and Bdp1p, directs pol III to the transcriptional start site of these genes and is itself recruited to a location immediately upstream of the transcriptional start site by the TFIIIC complex (38). TFIIIB binds to TFIIIC mainly through contact between TFIIIB subunits Brf1p and Bdp1p and the TFIIIC subunit Tfc4p, and between TBP and the TFIIIC subunit Tfc8p (39, 40). The TFIIIB footprint on promoter DNA is influenced by the DNA-binding site preferences of the TBP subunit and by the non-histone chromatin proteins Nhp6Ap and Nhp6bp (41 and reviewed in 42). TFIIIB function is also important for promoter opening (via the Brf1p and Bdp1p subunits), reinitiation of pol III transcription, and targeting and efficiency of Ty3 retrotransposition (43, 44, and 45). TFIIIB is also the target of Maf1-mediated repression of pol III transcription (reviewed in 46).

Last updated: 2005-11-15 Contact SGD

References cited on this page View Complete Literature Guide for SPT15
1) Roberts SM and Winston F  (1996) SPT20/ADA5 encodes a novel protein functionally related to the TATA-binding protein and important for transcription in Saccharomyces cerevisiae. Mol Cell Biol 16(6):3206-13
2) Yamaguchi Y, et al.  (2001) SPT genes: key players in the regulation of transcription, chromatin structure and other cellular processes. J Biochem 129(2):185-91
3) Cormack BP and Struhl K  (1992) The TATA-binding protein is required for transcription by all three nuclear RNA polymerases in yeast cells. Cell 69(4):685-96
4) Fan X, et al.  (2005) Distinct transcriptional responses of RNA polymerases I, II and III to aptamers that bind TBP. Nucleic Acids Res 33(3):838-45
5) Reeder RH  (1999) Regulation of RNA polymerase I transcription in yeast and vertebrates. Prog Nucleic Acid Res Mol Biol 62:293-327
6) Hampsey M  (1998) Molecular genetics of the RNA polymerase II general transcriptional machinery. Microbiol Mol Biol Rev 62(2):465-503
7) Geiduschek EP and Kassavetis GA  (2001) The RNA polymerase III transcription apparatus. J Mol Biol 310(1):1-26
8) Hahn S, et al.  (1989) Yeast TATA-binding protein TFIID binds to TATA elements with both consensus and nonconsensus DNA sequences. Proc Natl Acad Sci U S A 86(15):5718-22
9) Spencer JV and Arndt KM  (2002) A TATA binding protein mutant with increased affinity for DNA directs transcription from a reversed TATA sequence in vivo. Mol Cell Biol 22(24):8744-55
10) Leng P, et al.  (1998) The TATA-binding protein (TBP) from the human fungal pathogen Candida albicans can complement defects in human and yeast TBPs. J Bacteriol 180(7):1771-6
11) Nakamura K, et al.  (2001) SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein. Hum Mol Genet 10(14):1441-8
12) Schmidt MC, et al.  (1989) Yeast TATA-box transcription factor gene. Proc Natl Acad Sci U S A 86(20):7785-9
13) Lee M and Struhl K  (2001) Multiple functions of the nonconserved N-terminal domain of yeast TATA-binding protein. Genetics 158(1):87-93
14) Kim JL, et al.  (1993) Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature 365(6446):520-7
15) Kim TK and Roeder RG  (1994) Involvement of the basic repeat domain of TATA-binding protein (TBP) in transcription by RNA polymerases I, II, and III. J Biol Chem 269(7):4891-4
16) Kou H, et al.  (2003) Structural and functional analysis of mutations along the crystallographic dimer interface of the yeast TATA binding protein. Mol Cell Biol 23(9):3186-201
17) Coleman RA and Pugh BF  (1997) Slow dimer dissociation of the TATA binding protein dictates the kinetics of DNA binding. Proc Natl Acad Sci U S A 94(14):7221-6
18) Jackson-Fisher AJ, et al.  (1999) A role for TBP dimerization in preventing unregulated gene expression. Mol Cell 3(6):717-27
19) Huisinga KL and Pugh BF  (2004) A genome-wide housekeeping role for TFIID and a highly regulated stress-related role for SAGA in Saccharomyces cerevisiae. Mol Cell 13(4):573-85
20) Lewis BA and Reinberg D  (2003) The mediator coactivator complex: functional and physical roles in transcriptional regulation. J Cell Sci 116(Pt 18):3667-75
21) Darst RP, et al.  (2003) Mot1 regulates the DNA binding activity of free TATA-binding protein in an ATP-dependent manner. J Biol Chem 278(15):13216-26
22) Goppelt A and Meisterernst M  (1996) Characterization of the basal inhibitor of class II transcription NC2 from Saccharomyces cerevisiae. Nucleic Acids Res 24(22):4450-5
23) Steffan JS, et al.  (1998) Interaction of TATA-binding protein with upstream activation factor is required for activated transcription of ribosomal DNA by RNA polymerase I in Saccharomyces cerevisiae in vivo. Mol Cell Biol 18(7):3752-61
24) Steffan JS, et al.  (1996) The role of TBP in rDNA transcription by RNA polymerase I in Saccharomyces cerevisiae: TBP is required for upstream activation factor-dependent recruitment of core factor. Genes Dev 10(20):2551-63
25) Lalo D, et al.  (1996) RRN11 encodes the third subunit of the complex containing Rrn6p and Rrn7p that is essential for the initiation of rDNA transcription by yeast RNA polymerase I. J Biol Chem 271(35):21062-7
26) Tansey WP and Herr W  (1997) TAFs: guilt by association? Cell 88(6):729-32
27) Sanders SL, et al.  (2002) Molecular characterization of Saccharomyces cerevisiae TFIID. Mol Cell Biol 22(16):6000-13
28) Auty R, et al.  (2004) Purification of active TFIID from Saccharomyces cerevisiae. Extensive promoter contacts and co-activator function. J Biol Chem 279(48):49973-81
29) Sayre MH, et al.  (1992) Reconstitution of transcription with five purified initiation factors and RNA polymerase II from Saccharomyces cerevisiae. J Biol Chem 267(32):23376-82
30) Macpherson N, et al.  (2000) A yeast taf17 mutant requires the Swi6 transcriptional activator for viability and shows defects in cell cycle-regulated transcription. Genetics 154(4):1561-76
31) Kobayashi A, et al.  (2003) Mutations in the histone fold domain of the TAF12 gene show synthetic lethality with the TAF1 gene lacking the TAF N-terminal domain (TAND) by different mechanisms from those in the SPT15 gene encoding the TATA box-binding protein (TBP). Nucleic Acids Res 31(4):1261-74
32) Klebanow ER, et al.  (1996) Isolation and characterization of TAF25, an essential yeast gene that encodes an RNA polymerase II-specific TATA-binding protein-associated factor. J Biol Chem 271(23):13706-15
33) Walker SS, et al.  (1997) Yeast TAF(II)145 required for transcription of G1/S cyclin genes and regulated by the cellular growth state. Cell 90(4):607-14
34) Shen WC, et al.  (2003) Systematic analysis of essential yeast TAFs in genome-wide transcription and preinitiation complex assembly. EMBO J 22(13):3395-402
35) Buratowski S, et al.  (1989) Five intermediate complexes in transcription initiation by RNA polymerase II. Cell 56(4):549-61
36) Ranish JA and Hahn S  (1991) The yeast general transcription factor TFIIA is composed of two polypeptide subunits. J Biol Chem 266(29):19320-7
37) Li XY, et al.  (2002) Selective recruitment of TAFs by yeast upstream activating sequences. Implications for eukaryotic promoter structure. Curr Biol 12(14):1240-4
38) Kassavetis GA, et al.  (1997) Domains of the Brf component of RNA polymerase III transcription factor IIIB (TFIIIB): functions in assembly of TFIIIB-DNA complexes and recruitment of RNA polymerase to the promoter. Mol Cell Biol 17(9):5299-306
39) Chaussivert N, et al.  (1995) Complex interactions between yeast TFIIIB and TFIIIC. J Biol Chem 270(25):15353-8
40) Deprez E, et al.  (1999) A subunit of yeast TFIIIC participates in the recruitment of TATA-binding protein. Mol Cell Biol 19(12):8042-51
41) Kassavetis GA and Steiner DF  (2006) Nhp6 is a transcriptional initiation fidelity factor for RNA polymerase III transcription in vitro and in vivo. J Biol Chem 281(11):7445-51
42) Geiduschek EP  (2009) Without a license, or accidents waiting to happen. Annu Rev Biochem 78:1-28
43) Kassavetis GA, et al.  (2001) The RNA polymerase III transcription initiation factor TFIIIB participates in two steps of promoter opening. EMBO J 20(11):2823-34
44) Ferrari R, et al.  (2004) Distinct roles of transcription factors TFIIIB and TFIIIC in RNA polymerase III transcription reinitiation. Proc Natl Acad Sci U S A 101(37):13442-7
45) Yieh L, et al.  (2002) Mutational analysis of the transcription factor IIIB-DNA target of Ty3 retroelement integration. J Biol Chem 277(29):25920-8
46) Ciesla M and Boguta M  (2008) Regulation of RNA polymerase III transcription by Maf1 protein. Acta Biochim Pol 55(2):215-25
47) Zhu C, et al.  (2009) High-resolution DNA-binding specificity analysis of yeast transcription factors. Genome Res 19(4):556-66